PORB_ARATH
ID PORB_ARATH Reviewed; 401 AA.
AC P21218; B9DG36; Q42537; Q8LAV9;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protochlorophyllide reductase B, chloroplastic;
DE Short=PCR B;
DE EC=1.3.1.33;
DE AltName: Full=NADPH-protochlorophyllide oxidoreductase B;
DE Short=POR B;
DE Flags: Precursor;
GN Name=PORB; OrderedLocusNames=At4g27440; ORFNames=F27G19.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=7659751; DOI=10.1104/pp.108.4.1505;
RA Armstrong G.A., Runge S., Frick G., Sperling U., Apel K.;
RT "Identification of NADPH:protochlorophyllide oxidoreductases A and B: a
RT branched pathway for light-dependent chlorophyll biosynthesis in
RT Arabidopsis thaliana.";
RL Plant Physiol. 108:1505-1517(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT ASP-395.
RC STRAIN=cv. An-2; TISSUE=Leaf;
RX PubMed=1714319; DOI=10.1007/bf00023426;
RA Benli M., Schuelz R., Apel K.;
RT "Effect of light on the NADPH-protochlorophyllide oxidoreductase of
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 16:615-625(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12848821; DOI=10.1046/j.1365-313x.2003.01798.x;
RA Frick G., Su Q., Apel K., Armstrong G.A.;
RT "An Arabidopsis porB porC double mutant lacking light-dependent
RT NADPH:protochlorophyllide oxidoreductases B and C is highly chlorophyll-
RT deficient and developmentally arrested.";
RL Plant J. 35:141-153(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=10838072; DOI=10.1016/s0014-5793(00)01568-4;
RA Oosawa N., Masuda T., Awai K., Fusada N., Shimada H., Ohta H., Takamiya K.;
RT "Identification and light-induced expression of a novel gene of NADPH-
RT protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana.";
RL FEBS Lett. 474:133-136(2000).
RN [10]
RP FUNCTION, INDUCTION BY LIGHT, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11785941; DOI=10.1023/a:1013699721301;
RA Su Q., Frick G., Armstrong G., Apel K.;
RT "POR C of Arabidopsis thaliana: a third light- and NADPH-dependent
RT protochlorophyllide oxidoreductase that is differentially regulated by
RT light.";
RL Plant Mol. Biol. 47:805-813(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=15842619; DOI=10.1111/j.1365-313x.2005.02374.x;
RA Kim C., Ham H., Apel K.;
RT "Multiplicity of different cell- and organ-specific import routes for the
RT NADPH-protochlorophyllide oxidoreductases A and B in plastids of
RT Arabidopsis seedlings.";
RL Plant J. 42:329-340(2005).
RN [13]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP MEMBRANE COMPLEX.
RX PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT physically linked to the final steps of the Mg(++)-branch of this
RT pathway.";
RL FEBS Lett. 586:211-216(2012).
RN [14]
RP PYROGLUTAMATE FORMATION [LARGE SCALE ANALYSIS] AT GLN-67, CLEAVAGE OF
RP TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP INTERACTION WITH CDF1.
RC STRAIN=cv. Columbia;
RX PubMed=24151298; DOI=10.1105/tpc.113.111096;
RA Lee J.-Y., Lee H.-S., Song J.-Y., Jung Y.J., Reinbothe S., Park Y.-I.,
RA Lee S.Y., Pai H.-S.;
RT "Cell growth defect factor1/chaperone-like protein of POR1 plays a role in
RT stabilization of light-dependent protochlorophyllide oxidoreductase in
RT Nicotiana benthamiana and Arabidopsis.";
RL Plant Cell 25:3944-3960(2013).
CC -!- FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to
CC chlorophyllide (Chlide). {ECO:0000269|PubMed:11785941,
CC ECO:0000269|PubMed:12848821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH +
CC protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348,
CC ChEBI:CHEBI:83350; EC=1.3.1.33;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1 (PubMed:22212719).
CC Interacts with CDF1 in chloroplast (PubMed:24151298).
CC {ECO:0000269|PubMed:22212719, ECO:0000269|PubMed:24151298}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane. Plastid,
CC chloroplast thylakoid membrane.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, upper leaves, rosette and
CC cauline leaves, stem. Not detectable in non-photosynthetic tissues such
CC as roots and seeds. Expressed in seedlings and adult plant.
CC {ECO:0000269|PubMed:10838072}.
CC -!- DEVELOPMENTAL STAGE: Expressed in etiolated seedlings.
CC {ECO:0000269|PubMed:11785941}.
CC -!- INDUCTION: Circadian-regulation. Not regulated by light.
CC {ECO:0000269|PubMed:10838072, ECO:0000269|PubMed:11785941,
CC ECO:0000269|PubMed:7659751}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at the levels of the whole
CC plant or chloroplast ultrastructure; due to the redundancy with PORC.
CC Porb and porc double mutants have a seedling-lethal pale-yellow xantha
CC phenotype at the cotyledon stage, contain only small amounts of Chla,
CC and possess chloroplasts with mostly unstacked thylakoid membranes.
CC {ECO:0000269|PubMed:12848821}.
CC -!- MISCELLANEOUS: The presence of TOC33 is required for the import of PORA
CC into plastids in cotyledons and true leaves.
CC {ECO:0000305|PubMed:15842619}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. POR subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29785; AAC49044.1; -; mRNA.
DR EMBL; AL078467; CAB43876.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81394.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85342.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85343.1; -; Genomic_DNA.
DR EMBL; AY042883; AAK68823.1; -; mRNA.
DR EMBL; AY054206; AAL06867.1; -; mRNA.
DR EMBL; AY081465; AAM10027.1; -; mRNA.
DR EMBL; AK317009; BAH19703.1; -; mRNA.
DR EMBL; AY087574; AAM65116.1; -; mRNA.
DR PIR; T08936; T08936.
DR RefSeq; NP_001031731.1; NM_001036654.1.
DR RefSeq; NP_194474.1; NM_118879.4.
DR PDB; 7JK9; EM; 3.10 A; A/AA/B/BA/C/CA/D/DA/E/EA/F/FA/G/GA/H/HA/I/IA/J/JA/K/KA/L/LA/M/MA/N/NA/O/OA=1-401.
DR PDBsum; 7JK9; -.
DR AlphaFoldDB; P21218; -.
DR SMR; P21218; -.
DR BioGRID; 14140; 4.
DR IntAct; P21218; 3.
DR MINT; P21218; -.
DR STRING; 3702.AT4G27440.1; -.
DR iPTMnet; P21218; -.
DR PaxDb; P21218; -.
DR PRIDE; P21218; -.
DR ProteomicsDB; 250597; -.
DR EnsemblPlants; AT4G27440.1; AT4G27440.1; AT4G27440.
DR EnsemblPlants; AT4G27440.2; AT4G27440.2; AT4G27440.
DR GeneID; 828853; -.
DR Gramene; AT4G27440.1; AT4G27440.1; AT4G27440.
DR Gramene; AT4G27440.2; AT4G27440.2; AT4G27440.
DR KEGG; ath:AT4G27440; -.
DR Araport; AT4G27440; -.
DR TAIR; locus:2124044; AT4G27440.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_3_1; -.
DR InParanoid; P21218; -.
DR OMA; YWSWNNA; -.
DR OrthoDB; 1032903at2759; -.
DR PhylomeDB; P21218; -.
DR BioCyc; ARA:AT4G27440-MON; -.
DR BRENDA; 1.3.1.33; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:P21218; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P21218; baseline and differential.
DR Genevisible; P21218; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0016630; F:protochlorophyllide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005979; Prochl_reduct.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44419; PTHR44419; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01289; LPOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast;
KW Direct protein sequencing; Membrane; NADP; Oxidoreductase; Photosynthesis;
KW Plastid; Plastid outer membrane; Pyrrolidone carboxylic acid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 67..401
FT /note="Protochlorophyllide reductase B, chloroplastic"
FT /id="PRO_0000023288"
FT MOD_RES 67
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VARIANT 395
FT /note="E -> D (in strain: cv. An-2)"
FT CONFLICT 47
FT /note="G -> R (in Ref. 7; AAM65116)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="E -> Q (in Ref. 7; AAM65116)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="G -> A (in Ref. 7; AAM65116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43359 MW; 0C2132F980AF6CA3 CRC64;
MALQAASLVS SAFSVRKDAK LNASSSSFKD SSLFGASITD QIKSEHGSSS LRFKREQSLR
NLAIRAQTAA TSSPTVTKSV DGKKTLRKGN VVVTGASSGL GLATAKALAE TGKWNVIMAC
RDFLKAERAA KSVGMPKDSY TVMHLDLASL DSVRQFVDNF RRTETPLDVL VCNAAVYFPT
AKEPTYSAEG FELSVATNHL GHFLLARLLL DDLKKSDYPS KRLIIVGSIT GNTNTLAGNV
PPKANLGDLR GLAGGLNGLN SSAMIDGGDF DGAKAYKDSK VCNMLTMQEF HRRFHEETGV
TFASLYPGCI ASTGLFREHI PLFRALFPPF QKYITKGYVS ETESGKRLAQ VVSDPSLTKS
GVYWSWNNAS ASFENQLSEE ASDVEKARKV WEISEKLVGL A
